ID A0A151WNX3_9HYME Unreviewed; 836 AA.
AC A0A151WNX3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
GN ORFNames=ALC60_11420 {ECO:0000313|EMBL:KYQ49491.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ49491.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ49491.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ49491.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ49491.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Introduces a single-strand break via transesterification at a
CC target site in duplex DNA. Releases the supercoiling and torsional
CC tension of DNA introduced during the DNA replication and transcription
CC by transiently cleaving and rejoining one strand of the DNA duplex. The
CC scissile phosphodiester is attacked by the catalytic tyrosine of the
CC enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme
CC intermediate and the expulsion of a 3'-OH DNA strand.
CC {ECO:0000256|RuleBase:RU362092}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000213,
CC ECO:0000256|RuleBase:RU362092};
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|RuleBase:RU362092}.
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DR EMBL; KQ982905; KYQ49491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151WNX3; -.
DR STRING; 64791.A0A151WNX3; -.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR023406; Topo_IA_AS.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR013825; Topo_IA_cen_sub2.
DR InterPro; IPR013826; Topo_IA_cen_sub3.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR PANTHER; PTHR11390:SF20; DNA TOPOISOMERASE 3-BETA-1; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362092};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362092};
KW Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362092}.
FT DOMAIN 3..148
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 804..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 93831 MW; D49420748E43BBA5 CRC64;
MKTALMVAEK PSLAASLANI LSSGRCSTRK GLNGSCSVHE WVGQFRSETV NFKMTSVCGH
VMTLDFIGKY NNWDKVDPAE LFSCSTEKKE AVPKLKIPYF LAKEGAHCDY LVLWLDCDKE
GENICFEVDI WRARFSAITE KDIKSALANL IKPNENEAKS VDARQELDLR IGCAFTRYQT
KFFQGKYGDL DVSLISYGPC QTPTLGFCVQ RHDEIQTFKP DPYWVLQVTV KSPDGQDIVL
SWNRVRSFDK EVASMFLSHV KEHDQATVVS VQSTEKSKSR PIALNTVELM RVASSGLGMG
PQHAMQIAER LYTQGYISYP RTETTSYPEN FDLLSTLKQQ QSNSEWGEEV RKIIAAGINR
PKKGHDAGDH PPITPMKHAT RNELDGDLWR LYDYITRHFI ATLARDCRYL STTVKFEIGI
EIFTVTGHSL LSPGYTSILT WQALGNSDTL PKFMSDEKVN IQEAKLVECY TQPPDYLTEA
ELISLMEKHG IGTDASIPVH INNICIRNYV TVAAGRKLIP TSLGIVLVHG YQKIDPELVL
PTMRSAVEEQ LNLIALGRAD FYAVLQHTVE IFKQKFHYFV QSIEAMDQLF EVSFSPLSAS
GKAHSRCGKC RRYMKYIQTK PSRMHCAHCN ETYNLPQNGN IRIYKELKCP LDDFELLSWS
TGTRGKSYTF CPYCYNNPPF RDMKKGMSGC NSCTHPTCPH GMNSNGLSSC LECDLGILVL
DPSAAPKWKL GCNRCDVIIH LFENAHKVTV DTDTCDCGAQ LVTVEYKQDK SKLPNEATEM
SGCVFCTPAF AALVEKHRAV ASKPVVTRGR GHAKSRNRGK PKPPKDKMAQ LAAYFV
//